Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3J41

Pseudo-atomic model of the Aquaporin-0/Calmodulin complex derived from electron microscopy

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002088	biological_process	lens development in camera-type eye
A	0005212	molecular_function	structural constituent of eye lens
A	0005516	molecular_function	calmodulin binding
A	0005886	cellular_component	plasma membrane
A	0006833	biological_process	water transport
A	0007601	biological_process	visual perception
A	0015250	molecular_function	water channel activity
A	0015267	molecular_function	channel activity
A	0016020	cellular_component	membrane
A	0016324	cellular_component	apical plasma membrane
A	0034109	biological_process	homotypic cell-cell adhesion
A	0036438	biological_process	maintenance of lens transparency
A	0055085	biological_process	transmembrane transport
A	0070161	cellular_component	anchoring junction
A	0098631	molecular_function	cell adhesion mediator activity
A	1990349	biological_process	gap junction-mediated intercellular transport
B	0002088	biological_process	lens development in camera-type eye
B	0005212	molecular_function	structural constituent of eye lens
B	0005516	molecular_function	calmodulin binding
B	0005886	cellular_component	plasma membrane
B	0006833	biological_process	water transport
B	0007601	biological_process	visual perception
B	0015250	molecular_function	water channel activity
B	0015267	molecular_function	channel activity
B	0016020	cellular_component	membrane
B	0016324	cellular_component	apical plasma membrane
B	0034109	biological_process	homotypic cell-cell adhesion
B	0036438	biological_process	maintenance of lens transparency
B	0055085	biological_process	transmembrane transport
B	0070161	cellular_component	anchoring junction
B	0098631	molecular_function	cell adhesion mediator activity
B	1990349	biological_process	gap junction-mediated intercellular transport
C	0002088	biological_process	lens development in camera-type eye
C	0005212	molecular_function	structural constituent of eye lens
C	0005516	molecular_function	calmodulin binding
C	0005886	cellular_component	plasma membrane
C	0006833	biological_process	water transport
C	0007601	biological_process	visual perception
C	0015250	molecular_function	water channel activity
C	0015267	molecular_function	channel activity
C	0016020	cellular_component	membrane
C	0016324	cellular_component	apical plasma membrane
C	0034109	biological_process	homotypic cell-cell adhesion
C	0036438	biological_process	maintenance of lens transparency
C	0055085	biological_process	transmembrane transport
C	0070161	cellular_component	anchoring junction
C	0098631	molecular_function	cell adhesion mediator activity
C	1990349	biological_process	gap junction-mediated intercellular transport
D	0002088	biological_process	lens development in camera-type eye
D	0005212	molecular_function	structural constituent of eye lens
D	0005516	molecular_function	calmodulin binding
D	0005886	cellular_component	plasma membrane
D	0006833	biological_process	water transport
D	0007601	biological_process	visual perception
D	0015250	molecular_function	water channel activity
D	0015267	molecular_function	channel activity
D	0016020	cellular_component	membrane
D	0016324	cellular_component	apical plasma membrane
D	0034109	biological_process	homotypic cell-cell adhesion
D	0036438	biological_process	maintenance of lens transparency
D	0055085	biological_process	transmembrane transport
D	0070161	cellular_component	anchoring junction
D	0098631	molecular_function	cell adhesion mediator activity
D	1990349	biological_process	gap junction-mediated intercellular transport
E	0000086	biological_process	G2/M transition of mitotic cell cycle
E	0000922	cellular_component	spindle pole
E	0002027	biological_process	regulation of heart rate
E	0005246	molecular_function	calcium channel regulator activity
E	0005509	molecular_function	calcium ion binding
E	0005513	biological_process	detection of calcium ion
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005737	cellular_component	cytoplasm
E	0005813	cellular_component	centrosome
E	0005819	cellular_component	spindle
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0005876	cellular_component	spindle microtubule
E	0005886	cellular_component	plasma membrane
E	0005929	cellular_component	cilium
E	0007186	biological_process	G protein-coupled receptor signaling pathway
E	0007259	biological_process	cell surface receptor signaling pathway via JAK-STAT
E	0008076	cellular_component	voltage-gated potassium channel complex
E	0010856	molecular_function	adenylate cyclase activator activity
E	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
E	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
E	0016020	cellular_component	membrane
E	0016240	biological_process	autophagosome membrane docking
E	0019855	molecular_function	calcium channel inhibitor activity
E	0019901	molecular_function	protein kinase binding
E	0021762	biological_process	substantia nigra development
E	0030017	cellular_component	sarcomere
E	0030672	cellular_component	synaptic vesicle membrane
E	0031432	molecular_function	titin binding
E	0031514	cellular_component	motile cilium
E	0031982	cellular_component	vesicle
E	0032465	biological_process	regulation of cytokinesis
E	0032991	cellular_component	protein-containing complex
E	0034704	cellular_component	calcium channel complex
E	0035458	biological_process	cellular response to interferon-beta
E	0042995	cellular_component	cell projection
E	0043209	cellular_component	myelin sheath
E	0043539	molecular_function	protein serine/threonine kinase activator activity
E	0044305	cellular_component	calyx of Held
E	0044325	molecular_function	transmembrane transporter binding
E	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
E	0046872	molecular_function	metal ion binding
E	0048306	molecular_function	calcium-dependent protein binding
E	0050848	biological_process	regulation of calcium-mediated signaling
E	0051592	biological_process	response to calcium ion
E	0055117	biological_process	regulation of cardiac muscle contraction
E	0060291	biological_process	long-term synaptic potentiation
E	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
E	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
E	0071346	biological_process	cellular response to type II interferon
E	0072542	molecular_function	protein phosphatase activator activity
E	0097225	cellular_component	sperm midpiece
E	0097720	biological_process	calcineurin-mediated signaling
E	0098901	biological_process	regulation of cardiac muscle cell action potential
E	0099523	cellular_component	presynaptic cytosol
E	0140056	biological_process	organelle localization by membrane tethering
E	0140238	biological_process	presynaptic endocytosis
E	0141110	molecular_function	transporter inhibitor activity
E	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
E	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
E	1902494	cellular_component	catalytic complex
E	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
E	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering
F	0000086	biological_process	G2/M transition of mitotic cell cycle
F	0000922	cellular_component	spindle pole
F	0002027	biological_process	regulation of heart rate
F	0005246	molecular_function	calcium channel regulator activity
F	0005509	molecular_function	calcium ion binding
F	0005513	biological_process	detection of calcium ion
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005634	cellular_component	nucleus
F	0005654	cellular_component	nucleoplasm
F	0005737	cellular_component	cytoplasm
F	0005813	cellular_component	centrosome
F	0005819	cellular_component	spindle
F	0005829	cellular_component	cytosol
F	0005856	cellular_component	cytoskeleton
F	0005876	cellular_component	spindle microtubule
F	0005886	cellular_component	plasma membrane
F	0005929	cellular_component	cilium
F	0007186	biological_process	G protein-coupled receptor signaling pathway
F	0007259	biological_process	cell surface receptor signaling pathway via JAK-STAT
F	0008076	cellular_component	voltage-gated potassium channel complex
F	0010856	molecular_function	adenylate cyclase activator activity
F	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
F	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
F	0016020	cellular_component	membrane
F	0016240	biological_process	autophagosome membrane docking
F	0019855	molecular_function	calcium channel inhibitor activity
F	0019901	molecular_function	protein kinase binding
F	0021762	biological_process	substantia nigra development
F	0030017	cellular_component	sarcomere
F	0030672	cellular_component	synaptic vesicle membrane
F	0031432	molecular_function	titin binding
F	0031514	cellular_component	motile cilium
F	0031982	cellular_component	vesicle
F	0032465	biological_process	regulation of cytokinesis
F	0032991	cellular_component	protein-containing complex
F	0034704	cellular_component	calcium channel complex
F	0035458	biological_process	cellular response to interferon-beta
F	0042995	cellular_component	cell projection
F	0043209	cellular_component	myelin sheath
F	0043539	molecular_function	protein serine/threonine kinase activator activity
F	0044305	cellular_component	calyx of Held
F	0044325	molecular_function	transmembrane transporter binding
F	0046427	biological_process	positive regulation of receptor signaling pathway via JAK-STAT
F	0046872	molecular_function	metal ion binding
F	0048306	molecular_function	calcium-dependent protein binding
F	0050848	biological_process	regulation of calcium-mediated signaling
F	0051592	biological_process	response to calcium ion
F	0055117	biological_process	regulation of cardiac muscle contraction
F	0060291	biological_process	long-term synaptic potentiation
F	0060314	biological_process	regulation of ryanodine-sensitive calcium-release channel activity
F	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
F	0071346	biological_process	cellular response to type II interferon
F	0072542	molecular_function	protein phosphatase activator activity
F	0097225	cellular_component	sperm midpiece
F	0097720	biological_process	calcineurin-mediated signaling
F	0098901	biological_process	regulation of cardiac muscle cell action potential
F	0099523	cellular_component	presynaptic cytosol
F	0140056	biological_process	organelle localization by membrane tethering
F	0140238	biological_process	presynaptic endocytosis
F	0141110	molecular_function	transporter inhibitor activity
F	1901842	biological_process	negative regulation of high voltage-gated calcium channel activity
F	1901844	biological_process	regulation of cell communication by electrical coupling involved in cardiac conduction
F	1902494	cellular_component	catalytic complex
F	1905913	biological_process	negative regulation of calcium ion export across plasma membrane
F	1990456	biological_process	mitochondrion-endoplasmic reticulum membrane tethering

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA E 201

Chain	Residue
E	ASP20
E	ASP22
E	ASP24
E	THR26

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA E 202

Chain	Residue
E	ASP58
E	ASN60
E	THR62
E	ASP64

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 203

Chain	Residue
E	ASP95
E	ASN97
E	TYR99
E	GLU104
E	ASP93

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 204

Chain	Residue
E	ASP129
E	ASP131
E	ASP133
E	GLN135
E	GLU140

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA F 201

Chain	Residue
F	ASP20
F	ASP22
F	ASP24
F	THR26

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA F 202

Chain	Residue
F	ASP58
F	ASN60
F	THR62
F	ASP64

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 203

Chain	Residue
F	ASP93
F	ASP95
F	ASN97
F	TYR99
F	GLU104

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 204

Chain	Residue
F	ASP129
F	ASP131
F	ASP133
F	GLN135
F	GLU140

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL

Chain	Residue	Details
E	ASP20-LEU32
E	ASP56-PHE68
E	ASP93-LEU105
E	ASP129-PHE141

site_id	PS00107
Number of Residues	29
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGLGSLLYdFllfprlksvserl.....SILK

Chain	Residue	Details
A	ILE210-LYS238

site_id	PS00221
Number of Residues	9
Details	MIP MIP family signature. HVNPAVTFA

Chain	Residue	Details
A	HIS66-ALA74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	68
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	140
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	72
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	80
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	108
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	80
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	68
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	68
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	40
Details	Region: {"description":"Interaction with CALM","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Motif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	8
Details	Motif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Site: {"description":"Important for water channel gating","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Site: {"description":"Cleavage; promotes interactions between tetramers from adjoining membranes","evidences":[{"source":"PubMed","id":"15351655","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	70
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	70
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	70
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	64
Details	Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	144
Details	Region: {"description":"Necessary and sufficient for interaction with PCP4","evidences":[{"source":"PubMed","id":"27876793","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)